ID   BAEE_BACVZ              Reviewed;         746 AA.
AC   A7Z4Y0;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Polyketide biosynthesis protein BaeE;
DE   Includes:
DE     RecName: Full=Malonyl CoA-acyl carrier protein transacylase;
DE              Short=MCT;
DE              EC=2.3.1.39;
GN   Name=baeE; OrderedLocusNames=RBAM_016930;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
RN   [2]
RP   PATHWAY, AND FUNCTION IN BACILLAENE BIOSYNTHESIS.
RX   PubMed=16707694; DOI=10.1128/jb.00052-06;
RA   Chen X.-H., Vater J., Piel J., Franke P., Scholz R., Schneider K.,
RA   Koumoutsi A., Hitzeroth G., Grammel N., Strittmatter A.W., Gottschalk G.,
RA   Suessmuth R.D., Borriss R.;
RT   "Structural and functional characterization of three polyketide synthase
RT   gene clusters in Bacillus amyloliquefaciens FZB 42.";
RL   J. Bacteriol. 188:4024-4036(2006).
CC   -!- FUNCTION: Probably involved in some intermediate steps for the
CC       synthesis of the antibiotic polyketide bacillaene which is involved in
CC       secondary metabolism. Probably has an acyl transferase activity and
CC       could also have a flavin mononucleotide-dependent oxidoreductase
CC       activity. {ECO:0000269|PubMed:16707694}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC         Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449; EC=2.3.1.39;
CC   -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC       {ECO:0000269|PubMed:16707694}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the FabD family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000560; ABS74056.1; -; Genomic_DNA.
DR   RefSeq; WP_012117591.1; NC_009725.2.
DR   AlphaFoldDB; A7Z4Y0; -.
DR   SMR; A7Z4Y0; -.
DR   KEGG; bay:RBAM_016930; -.
DR   HOGENOM; CLU_008708_0_0_9; -.
DR   UniPathway; UPA01003; -.
DR   Proteomes; UP000001120; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd04742; NPD_FabD; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR049489; FabD-like_helical_ins.
DR   InterPro; IPR004410; Malonyl_CoA-ACP_transAc_FabD.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR014179; PfaD-like_TIM-barrel.
DR   NCBIfam; TIGR00128; fabD; 1.
DR   NCBIfam; TIGR02814; pfaD_fam; 1.
DR   PANTHER; PTHR42681; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42681:SF1; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF21607; FabD_helical_ins; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Antibiotic biosynthesis; Cytoplasm; Transferase.
FT   CHAIN           1..746
FT                   /note="Polyketide biosynthesis protein BaeE"
FT                   /id="PRO_0000388001"
FT   REGION          1..312
FT                   /note="Acyl transferase"
FT   ACT_SITE        85
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        191
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   746 AA;  82426 MW;  DCD623E4D0531171 CRC64;
     MISFVFPGQG SQRIGMGEDL FGRYPELTAK ADHILGYSIQ ELCRDGERLN QTQFTQPALY
     VVNALSYLKK TEETGLKPDF TAGHSLGEYN ALYASGAFDF EEGLQLVKKR GELMSRAKGG
     GMAAVIGLTH EQVTDVLREN HLDMIDIANM NTPQQIVISG YKEDIEKAAS VFEAVNGVKM
     VHRLNVSGAF HSRYMLEAKE EFSRFIESFH FKPLSIPVIS NVTARPYEQR ELKETLTGQI
     TGSVNWTDSI RFLMGRKNMS FEEIGPGKVL TGLIQRITAE AEPITDEIKV PAEAGKSSIT
     AASLGNEEFK RDYQLKYAYL AGGMYRGISS KEMVVKLAEK GMMGFFGTGG LNIAHVEDAI
     LSIQHELRDG GSFGINVVHN MKHTDSEEKM IDLLLKHGIQ NLEASAFLTV TPALVRFRAK
     GLKRGAGGQI IARQRIIAKL SRPEVAEAFL SPAPDHILQK LAAENKITAE EASLMREIPV
     AHDICVEADS GGHTDGGVAY SLMPAIIRLR DDMMKKYRYG KTVRIGAAGG IGTPEAAMAA
     FMLGADFIVT GSINQCTVEA ATSGLVKDLL QQMNVQDTAY APAGDMFESG SKVQVLKKGL
     FFPTRASKLH ELYQRHRSIE EIDEKTLRQI EEKYFKASVS SIYDKVKAHY SNEDISKAER
     NPKEKMALIF KWYFRQSSAS AIKGDPDAKV DFQIHCGPAL GAFNQWVKGT ELESWKNRHA
     DGIGMRLMEE TASLLNQKLG SFLQTC
//